Endoplasmic Reticulum Unfolded Protein Response, Aging and Exercise: An Update
The endoplasmic reticulum (ER) is a dynamic and multifunctional organelle responsible for protein biosynthesis, folding, assembly and modifications. Loss of protein folding regulation, which leads to unfolded or misfolded proteins accumulation inside the ER lumen, drives ER stress (ERS) and unfolded...
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| Published in | Frontiers in physiology Vol. 9; p. 1744 |
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| Main Authors | , , , |
| Format | Journal Article |
| Language | English |
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05.12.2018
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| Abstract | The endoplasmic reticulum (ER) is a dynamic and multifunctional organelle responsible for protein biosynthesis, folding, assembly and modifications. Loss of protein folding regulation, which leads to unfolded or misfolded proteins accumulation inside the ER lumen, drives ER stress (ERS) and unfolded protein response (UPR) activation. During aging, there is a decline in the ability of the cell to handle protein folding, accumulation and aggregation, and the function of UPR is compromised. There is a progressive failure of the chaperoning systems and a decline in many of its components, so that the UPR activation cannot rescue the ERS. Physical activity has been proposed as a powerful tool against aged-related diseases, which are linked to ERS. Interventional studies have demonstrated that regular exercise is able to decrease oxidative stress and inflammation and reverse mitochondrial and ER dysfunctions. Exercise-induced metabolic stress could activate the UPR since muscle contraction is directly involved in its activation, mediating exercise-induced adaptation responses. In fact, regular moderate-intensity exercise-induced ERS acts as a protective mechanism against current and future stressors. However, biological responses vary according to exercise intensity and therefore induce different degrees of ERS and UPR activation. This article reviews the effects of aging and exercise on ERS and UPR, also analyzing possible changes induced by different types of exercise in elderly subjects. |
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| AbstractList | The endoplasmic reticulum (ER) is a dynamic and multifunctional organelle responsible for protein biosynthesis, folding, assembly and modifications. Loss of protein folding regulation, which leads to unfolded or misfolded proteins accumulation inside the ER lumen, drives ER stress (ERS) and unfolded protein response (UPR) activation. During aging, there is a decline in the ability of the cell to handle protein folding, accumulation and aggregation, and the function of UPR is compromised. There is a progressive failure of the chaperoning systems and a decline in many of its components, so that the UPR activation cannot rescue the ERS. Physical activity has been proposed as a powerful tool against aged-related diseases, which are linked to ERS. Interventional studies have demonstrated that regular exercise is able to decrease oxidative stress and inflammation and reverse mitochondrial and ER dysfunctions. Exercise-induced metabolic stress could activate the UPR since muscle contraction is directly involved in its activation, mediating exercise-induced adaptation responses. In fact, regular moderate-intensity exercise-induced ERS acts as a protective mechanism against current and future stressors. However, biological responses vary according to exercise intensity and therefore induce different degrees of ERS and UPR activation. This article reviews the effects of aging and exercise on ERS and UPR, also analyzing possible changes induced by different types of exercise in elderly subjects.The endoplasmic reticulum (ER) is a dynamic and multifunctional organelle responsible for protein biosynthesis, folding, assembly and modifications. Loss of protein folding regulation, which leads to unfolded or misfolded proteins accumulation inside the ER lumen, drives ER stress (ERS) and unfolded protein response (UPR) activation. During aging, there is a decline in the ability of the cell to handle protein folding, accumulation and aggregation, and the function of UPR is compromised. There is a progressive failure of the chaperoning systems and a decline in many of its components, so that the UPR activation cannot rescue the ERS. Physical activity has been proposed as a powerful tool against aged-related diseases, which are linked to ERS. Interventional studies have demonstrated that regular exercise is able to decrease oxidative stress and inflammation and reverse mitochondrial and ER dysfunctions. Exercise-induced metabolic stress could activate the UPR since muscle contraction is directly involved in its activation, mediating exercise-induced adaptation responses. In fact, regular moderate-intensity exercise-induced ERS acts as a protective mechanism against current and future stressors. However, biological responses vary according to exercise intensity and therefore induce different degrees of ERS and UPR activation. This article reviews the effects of aging and exercise on ERS and UPR, also analyzing possible changes induced by different types of exercise in elderly subjects. The endoplasmic reticulum (ER) is a dynamic and multifunctional organelle responsible for protein biosynthesis, folding, assembly and modifications. Loss of protein folding regulation, which leads to unfolded or misfolded proteins accumulation inside the ER lumen, drives ER stress (ERS) and unfolded protein response (UPR) activation. During aging, there is a decline in the ability of the cell to handle protein folding, accumulation and aggregation, and the function of UPR is compromised. There is a progressive failure of the chaperoning systems and a decline in many of its components, so that the UPR activation cannot rescue the ERS. Physical activity has been proposed as a powerful tool against aged-related diseases, which are linked to ERS. Interventional studies have demonstrated that regular exercise is able to decrease oxidative stress and inflammation and reverse mitochondrial and ER dysfunctions. Exercise-induced metabolic stress could activate the UPR since muscle contraction is directly involved in its activation, mediating exercise-induced adaptation responses. In fact, regular moderate-intensity exercise-induced ERS acts as a protective mechanism against current and future stressors. However, biological responses vary according to exercise intensity and therefore induce different degrees of ERS and UPR activation. This article reviews the effects of aging and exercise on ERS and UPR, also analyzing possible changes induced by different types of exercise in elderly subjects. |
| Author | Cuevas, María J. González-Gallego, Javier de Paz, José A. Estébanez, Brisamar |
| AuthorAffiliation | 1 Institute of Biomedicine (IBIOMED), University of León , León , Spain 2 Centro de Investigación Biomédica en Red de Enfermedades Hepáticas y Digestivas (CIBERehd) , Madrid , Spain |
| AuthorAffiliation_xml | – name: 1 Institute of Biomedicine (IBIOMED), University of León , León , Spain – name: 2 Centro de Investigación Biomédica en Red de Enfermedades Hepáticas y Digestivas (CIBERehd) , Madrid , Spain |
| Author_xml | – sequence: 1 givenname: Brisamar surname: Estébanez fullname: Estébanez, Brisamar – sequence: 2 givenname: José A. surname: de Paz fullname: de Paz, José A. – sequence: 3 givenname: María J. surname: Cuevas fullname: Cuevas, María J. – sequence: 4 givenname: Javier surname: González-Gallego fullname: González-Gallego, Javier |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/30568599$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.18632/aging.100620 10.1016/j.neurobiolaging.2005.05.010 10.1242/jeb.125104 10.1152/japplphysiol.00021.2008 10.1016/j.lfs.2015.12.037 10.1007/s11357-016-9897-y 10.1016/j.tcm.2014.10.013 10.18632/aging.100879 10.1111/acel.12158 10.1002/biof.1280 10.1007/s13105-012-0204-9 10.1016/j.metabol.2016.06.004 10.1007/s00223-014-9944-6 10.1074/jbc.M300677200 10.1016/j.bbrc.2015.11.019 10.1139/apnm-2016-0542 10.1093/gerona/61.5.435 10.1016/j.exger.2004.02.008 10.1016/j.cmet.2011.01.003 10.1016/j.freeradbiomed.2016.08.017 10.1152/japplphysiol.01408.2010 10.1152/ajpcell.00240.2012 10.1111/jpi.12264 10.1007/s11357-014-9734-0 10.1016/j.mad.2015.08.002 10.1152/ajpregu.00511.2013 10.1016/j.ceca.2011.10.003 10.1007/s00421-010-1802-2 10.1016/j.neurobiolaging.2013.12.005 10.1007/s12035-014-9029-6 10.3892/ijmm_00000052 10.1016/j.arr.2009.03.001 10.2353/ajpath.2010.090386 10.1152/ajpcell.00009.2016 10.1111/j.1474-9726.2011.00699.x 10.4196/kjpp.2014.18.3.211 10.1123/ijsnem.11.s1.s9 10.1016/j.metabol.2015.02.003 10.1165/rcmb.2011-0224OC 10.1016/j.tibs.2015.01.002 10.1371/journal.pone.0050407 10.5717/jenb.2015.15080705 10.1016/S0006-291X(03)00826-X 10.1016/j.brainres.2009.12.062 10.1523/JNEUROSCI.5685-07.2008 10.1515/REVNEURO.2009.20.1.23 10.1093/gerona/glw063 10.1016/j.bbi.2016.05.010 10.1111/jcmm.12894 10.1016/j.ajpath.2013.05.026 10.1093/gerona/glu186 10.1016/j.bbrc.2007.01.156 10.1016/j.canlet.2015.02.029 10.1089/ars.2016.6671 10.1002/cbf.1643 10.18632/aging.101167 10.1007/s10495-013-0884-9 10.1155/2017/2049217 |
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| Copyright | Copyright © 2018 Estébanez, de Paz, Cuevas and González-Gallego. 2018 Estébanez, de Paz, Cuevas and González-Gallego |
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| Keywords | unfolded protein response exercise training aging elderly endoplasmic reticulum stress |
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| References | Gavilán (B15) 2006; 27 Memme (B33) 2016; 310 Senft (B50) 2015; 40 Rajesh (B47) 2013; 5 da Luz (B9) 2011; 111 Meijering (B30) 2015; 25 Huang (B18) 2015; 360 Drummond (B11) 2008; 104 Cai (B4) 2016; 57 Ghosh (B16) 2015; 70 Crespo (B8) 2012; 7 Pinto (B45) 2017; 42 Kim (B27) 2014; 18 Pereira (B44) 2016; 145 Torres-González (B55) 2012; 46 Jozsi (B23) 2001; 11 Rodriguez-Miguelez (B49) 2015; 150 Hussain (B20) 2007; 355 Rabek (B46) 2003; 305 Khadir (B26) 2016; 65 Ikeyama (B21) 2003; 278 Mejías-Peña (B31) 2017; 9 Naidoo (B39) 2011; 10 Chalil (B6); 468 Ogborn (B41) 2014; 307 Naidoo (B38) 2008; 28 Kang (B25) 2015; 19 O'Leary (B42) 2013; 304 Wu (B57) 2011; 13 Mejías-Peña (B32) 2016; 38 Passos (B43) 2015; 64 Mihailidou (B34) 2017; 27 Naidoo (B35); 8 Hong (B17) 2017; 2017 Naidoo (B36); 20 Baehr (B1) 2016; 8 Bozi (B2) 2016; 20 Kim (B28) 2010; 1317 Naidoo (B37) 2014; 13 Chapados (B7) 2010; 28 Deldicque (B10) 2013; 69 Brown (B3) 2014; 35 Drummond (B12) 2011; 111 Li (B29) 2004; 39 Nakka (B40) 2016; 53 Hulmi (B19) 2016; 99 Tamura (B54) 2017; 72 Fernández (B14) 2015; 59 Rodriguez-Miguelez (B48) 2014; 36 Smiles (B51) 2016; 219 Wu (B58) 2010; 176 Sreedhar (B52) 2016; 42 Chalil (B5); 96 Kang (B24) 2013; 18 Takeda (B53) 2013; 183 Um (B56) 2008; 22 Jiao (B22) 2012; 51 Erickson (B13) 2006; 61 |
| References_xml | – volume: 5 start-page: 884 year: 2013 ident: B47 article-title: eIF2α phosphorylation bypasses premature senescence caused by oxidative stress and pro-oxidant antitumor therapies publication-title: Aging doi: 10.18632/aging.100620 – volume: 27 start-page: 973 year: 2006 ident: B15 article-title: Cellular environment facilitates protein accumulation in aged rat hippocampus publication-title: Neurobiol. Aging doi: 10.1016/j.neurobiolaging.2005.05.010 – volume: 219 start-page: 214 year: 2016 ident: B51 article-title: Effects of skeletal muscle energy availability on protein turnover responses to exercise publication-title: J. Exp. Biol doi: 10.1242/jeb.125104 – volume: 104 start-page: 1452 year: 2008 ident: B11 article-title: Skeletal muscle protein anabolic response to resistance exercise essential amino acids is delayed with aging publication-title: J. Appl. Physiol. doi: 10.1152/japplphysiol.00021.2008 – volume: 145 start-page: 144 year: 2016 ident: B44 article-title: Excessive eccentric exercise-induced overtraining model leads to endoplasmic reticulum stress in mice skeletal muscles publication-title: Life Sci. doi: 10.1016/j.lfs.2015.12.037 – volume: 38 start-page: 33 year: 2016 ident: B32 article-title: Effects of aerobic training on markers of autophagy in the elderly publication-title: Age doi: 10.1007/s11357-016-9897-y – volume: 25 start-page: 243 year: 2015 ident: B30 article-title: Reviving the protein quality control system: therapeutic target for cardiac disease in the elderly publication-title: Trends Cardiovasc. Med. doi: 10.1016/j.tcm.2014.10.013 – volume: 8 start-page: 127 year: 2016 ident: B1 article-title: Age-related deficits in skeletal muscle recovery following disuse are associated with neuromuscular junction instability and ER stress, not impaired protein synthesis publication-title: Aging doi: 10.18632/aging.100879 – volume: 13 start-page: 131 year: 2014 ident: B37 article-title: Aging and sleep deprivation induce the unfolded protein response in the pancreas: implications for metabolism publication-title: Aging Cell doi: 10.1111/acel.12158 – volume: 42 start-page: 368 year: 2016 ident: B52 article-title: Role of MAPK-mediated endoplasmic reticulum stress signaling in the heart during aging in senescence-accelerated prone mice publication-title: Biofactors doi: 10.1002/biof.1280 – volume: 69 start-page: 215 year: 2013 ident: B10 article-title: Endurance training in mice increases the unfolded protein response induced by a high-fat diet publication-title: J. Physiol. Biochem. doi: 10.1007/s13105-012-0204-9 – volume: 65 start-page: 1409 year: 2016 ident: B26 article-title: Physical exercise alleviates ER stress in obese humans through reduction in the expression and release of GRP78 chaperone publication-title: Metabolism doi: 10.1016/j.metabol.2016.06.004 – volume: 96 start-page: 123 ident: B5 article-title: Increased endoplasmic reticulum stress in mouse osteocytes with aging alters Cox-2 response to mechanical stimuli publication-title: Calcif. Tissue Int. doi: 10.1007/s00223-014-9944-6 – volume: 278 start-page: 16726 year: 2003 ident: B21 article-title: Expression of the pro-apoptotic gene gadd153/chop is elevated in liver with aging and sensitizes cells to oxidant injury publication-title: J. Biol. Chem. doi: 10.1074/jbc.M300677200 – volume: 468 start-page: 702 ident: B6 article-title: Aging related ER stress is not responsible for anabolic resistance in mouse skeletal muscle publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2015.11.019 – volume: 42 start-page: 354 year: 2017 ident: B45 article-title: Excessive training is associated with endoplasmic reticulum stress but not apoptosis in the hypothalamus of mice publication-title: Appl. Physiol. Nutr. Metab. doi: 10.1139/apnm-2016-0542 – volume: 61 start-page: 435 year: 2006 ident: B13 article-title: The effect of aging on the chaperone concentrations in the hepatic, endoplasmic reticulum of male rats: the possible role of protein misfolding due to the loss of chaperones in the decline in physiological function seen with age publication-title: J. Gerontol. A Biol. Sci. Med. Sci. doi: 10.1093/gerona/61.5.435 – volume: 39 start-page: 735 year: 2004 ident: B29 article-title: Elevated gadd153/chop expression and enhanced c-Jun N-terminal protein kinase activation sensitizes aged cells to ER stress publication-title: Exp. Gerontol. doi: 10.1016/j.exger.2004.02.008 – volume: 13 start-page: 160 year: 2011 ident: B57 article-title: The unfolded protein response mediates adaptation to exercise in skeletal muscle through a PGC-1α/ATF6α complex publication-title: Cell Metab. doi: 10.1016/j.cmet.2011.01.003 – volume: 99 start-page: 308 year: 2016 ident: B19 article-title: Effects of muscular dystrophy, exercise and blocking activin receptor IIB ligands on the unfolded protein response and oxidative stress publication-title: Free Radic. Biol. Med. doi: 10.1016/j.freeradbiomed.2016.08.017 – volume: 111 start-page: 135 year: 2011 ident: B12 article-title: Skeletal muscle amino acid transporter expression is increased in young and older adults following resistance exercise publication-title: J. Appl. Physiol. doi: 10.1152/japplphysiol.01408.2010 – volume: 304 start-page: C422 year: 2013 ident: B42 article-title: Adaptive plasticity of autophagic proteins to denervation in aging skeletal muscle publication-title: Am. J. Physiol. Cell Physiol. doi: 10.1152/ajpcell.00240.2012 – volume: 59 start-page: 292 year: 2015 ident: B14 article-title: Melatonin and endoplasmic reticulum stress: relation to autophagy and apoptosis publication-title: J. Pineal Res doi: 10.1111/jpi.12264 – volume: 36 start-page: 9734 year: 2014 ident: B48 article-title: Role of Toll-like receptor 2 and 4 signaling pathways on the inflammatory response to resistance training in elderly subjects publication-title: Age doi: 10.1007/s11357-014-9734-0 – volume: 150 start-page: 12 year: 2015 ident: B49 article-title: Whole-body vibration improves the anti-inflammatory status in elderly subjects through toll-like receptor 2 and 4 signaling pathways publication-title: Mech. Ageing Dev. doi: 10.1016/j.mad.2015.08.002 – volume: 307 start-page: R664 year: 2014 ident: B41 article-title: The unfolded protein response is triggered following a single, unaccustomed resistance-exercise bout publication-title: Am. J. Physiol. Regul. Integr. Comp. Physiol. doi: 10.1152/ajpregu.00511.2013 – volume: 51 start-page: 31 year: 2012 ident: B22 article-title: Sarcalumenin plays a critical role in age-related cardiac dysfunction due to decreases in SERCA2a expression and activity publication-title: Cell Calcium doi: 10.1016/j.ceca.2011.10.003 – volume: 111 start-page: 2015 year: 2011 ident: B9 article-title: Endurance exercise training ameliorates insulin resistance and reticulum stress in adipose and hepatic tissue in obese rats publication-title: Eur. J. Appl. Physiol. doi: 10.1007/s00421-010-1802-2 – volume: 35 start-page: 1431 year: 2014 ident: B3 article-title: Aging induced endoplasmic reticulum stress alters sleep and sleep homeostasis publication-title: Neurobiol. Aging doi: 10.1016/j.neurobiolaging.2013.12.005 – volume: 53 start-page: 532 year: 2016 ident: B40 article-title: Crosstalk between endoplasmic reticulum stress, oxidative stress, and autophagy: potential therapeutic targets for acute CNS injuries publication-title: Mol. Neurobiol. doi: 10.1007/s12035-014-9029-6 – volume: 22 start-page: 529 year: 2008 ident: B56 article-title: Exercise training acts as a therapeutic strategy for reduction of the pathogenic phenotypes for Alzheimer's disease in an NSE/APPsw-transgenic model publication-title: Int. J. Mol. Med doi: 10.3892/ijmm_00000052 – volume: 8 start-page: 150 ident: B35 article-title: ER and aging-protein folding and the ER stress response publication-title: Ageing Res. Rev. doi: 10.1016/j.arr.2009.03.001 – volume: 176 start-page: 2163 year: 2010 ident: B58 article-title: Induction of diabetes in aged C57B6 mice results in severe nephropathy: an association with oxidative stress, endoplasmic reticulum stress, and inflammation publication-title: Am. J. Pathol. doi: 10.2353/ajpath.2010.090386 – volume: 310 start-page: C1024 year: 2016 ident: B33 article-title: Chronology of UPR activation in skeletal muscle adaptations to chronic contractile activity publication-title: Am. J. Physiol. Cell Physiol. doi: 10.1152/ajpcell.00009.2016 – volume: 10 start-page: 640 year: 2011 ident: B39 article-title: Endoplasmic reticulum stress in wake-active neurons progresses with aging publication-title: Aging Cell doi: 10.1111/j.1474-9726.2011.00699.x – volume: 18 start-page: 211 year: 2014 ident: B27 article-title: Effect of exercise intensity on unfolded protein response in skeletal muscle of rat publication-title: Korean J. Physiol. Pharmacol. doi: 10.4196/kjpp.2014.18.3.211 – volume: 11 start-page: S9 year: 2001 ident: B23 article-title: Molecular characteristics of aged muscle reflect an altered ability to respond to exercise publication-title: Int. J. Sport Nutr. Exerc. Metab doi: 10.1123/ijsnem.11.s1.s9 – volume: 64 start-page: 780 year: 2015 ident: B43 article-title: Endoplasmic reticulum stress response in non-alcoholic steatohepatitis: The possible role of physical exercise publication-title: Metabolism doi: 10.1016/j.metabol.2015.02.003 – volume: 46 start-page: 748 year: 2012 ident: B55 article-title: Role of endoplasmic reticulum stress in age-related susceptibility to lung fibrosis publication-title: Am. J. Respir. Cell Mol. Biol. doi: 10.1165/rcmb.2011-0224OC – volume: 40 start-page: 141 year: 2015 ident: B50 article-title: UPR, autophagy, and mitochondria crosstalk underlies the ER stress response publication-title: Trends Biochem. Sci doi: 10.1016/j.tibs.2015.01.002 – volume: 7 start-page: e50407 year: 2012 ident: B8 article-title: Glutamine treatment attenuates endoplasmic reticulum stress and apoptosis in TNBS-induced colitis publication-title: PLoS ONE doi: 10.1371/journal.pone.0050407 – volume: 19 start-page: 191 year: 2015 ident: B25 article-title: Exercise copes with prolonged stress-induced impairment of spatial memory performance by endoplasmic reticulum stress publication-title: J. Exerc. Nutr. Biochem. doi: 10.5717/jenb.2015.15080705 – volume: 305 start-page: 566 year: 2003 ident: B46 article-title: Carbonylation of ER chaperone proteins in aged mouse liver publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/S0006-291X(03)00826-X – volume: 1317 start-page: 13 year: 2010 ident: B28 article-title: Three weeks voluntary running wheel exercise increases endoplasmic reticulum stress in the brain of mice publication-title: Brain Res. doi: 10.1016/j.brainres.2009.12.062 – volume: 28 start-page: 6539 year: 2008 ident: B38 article-title: Aging impairs the unfolded protein response to sleep deprivation and leads to proapoptotic signaling publication-title: J. Neurosci. doi: 10.1523/JNEUROSCI.5685-07.2008 – volume: 20 start-page: 23 ident: B36 article-title: The endoplasmic reticulum stress response and aging publication-title: Rev. Neurosci. doi: 10.1515/REVNEURO.2009.20.1.23 – volume: 72 start-page: 299 year: 2017 ident: B54 article-title: Effects of heat stress treatment on age-dependent unfolded protein response in different types of skeletal muscle publication-title: J. Gerontol. A Biol. Sci. Med. Sci. doi: 10.1093/gerona/glw063 – volume: 57 start-page: 347 year: 2016 ident: B4 article-title: The signaling mechanisms of hippocampal endoplasmic reticulum stress affecting neuronal plasticity-related protein levels in high fat diet-induced obese rats and the regulation of aerobic exercise publication-title: Brain Behav. Immun. doi: 10.1016/j.bbi.2016.05.010 – volume: 20 start-page: 2208 year: 2016 ident: B2 article-title: Aerobic exercise training rescues cardiac protein quality control and blunts endoplasmic reticulum stress in heart failure rats publication-title: J. Cell. Mol. Med doi: 10.1111/jcmm.12894 – volume: 183 start-page: 774 year: 2013 ident: B53 article-title: Altered unfolded protein response is implicated in the age-related exacerbation of proteinuria-induced proximal tubular cell damage publication-title: Am. J. Pathol. doi: 10.1016/j.ajpath.2013.05.026 – volume: 70 start-page: 1320 year: 2015 ident: B16 article-title: Elevated endoplasmic reticulum stress response contributes to adipose tissue inflammation in aging publication-title: J. Gerontol. A Biol. Sci. Med. Sci. doi: 10.1093/gerona/glu186 – volume: 355 start-page: 365 year: 2007 ident: B20 article-title: Reduced eIF2alpha phosphorylation and increased proapoptotic proteins in aging publication-title: Biochem. Biophys. Res. Commun doi: 10.1016/j.bbrc.2007.01.156 – volume: 360 start-page: 257 year: 2015 ident: B18 article-title: Disruption of the unfolded protein response (UPR) by lead compound selectively suppresses cancer cell growth publication-title: Cancer Lett. doi: 10.1016/j.canlet.2015.02.029 – volume: 27 start-page: 185 year: 2017 ident: B34 article-title: Modulation of pancreatic islets' function and survival during aging involves the differential regulation of endoplasmic reticulum stress by p21 and CHOP publication-title: Antioxid. Redox Signal. doi: 10.1089/ars.2016.6671 – volume: 28 start-page: 202 year: 2010 ident: B7 article-title: Exercise training increases hepatic endoplasmic reticulum (er) stress protein expression in MTP-inhibited high-fat fed rats publication-title: Cell Biochem. Funct. doi: 10.1002/cbf.1643 – volume: 9 start-page: 408 year: 2017 ident: B31 article-title: Impact of resistance training on the autophagy-inflammation-apoptosis crosstalk in elderly subjects publication-title: Aging doi: 10.18632/aging.101167 – volume: 18 start-page: 1332 year: 2013 ident: B24 article-title: Treadmill exercise represses neuronal cell death and inflammation during Aβ-induced ER stress by regulating unfolded protein response in aged presenilin 2 mutant mice publication-title: Apoptosis doi: 10.1007/s10495-013-0884-9 – volume: 2017 start-page: 2049217 year: 2017 ident: B17 article-title: The role of endoplasmic reticulum stress in cardiovascular disease and exercise publication-title: Int. J. Vasc. Med doi: 10.1155/2017/2049217 |
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| Title | Endoplasmic Reticulum Unfolded Protein Response, Aging and Exercise: An Update |
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